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OLD AND NEW VIEWS OF PROTEIN FOLDING
Old and New Views of Protein FoldingProceedings of the 24th Taniguchi International Symposium, Division of Biophysics, Kisarazu, Japan, 3-7 March 1999

Edited by
K. Kuwajima, University of Tokyo, School of Science, Department of Physics, 7-3-1 Hongo, Bunkyo-ku, Tokyo 113-0033, Japan
M. Arai, University of Tokyo, School of Science, Department of Physics, 7-3-1 Hongo, Bunkyo-ku, Tokyo 113-0033, Japan

Included in series
International Congress, 1194

Description
Elucidation of protein folding mechanisms is a fundamental problem of molecular biological physics. During the last several years, remarkable advances have been made in this field. Experimentally, folding intermediates have been characterized in detail using various new techniques, and certain small proteins are found to fold in a two-state manner. Theoretical studies of simple model proteins have put forward new ideas of folding, and recent progress in computational techniques has made unfolding/folding simulations very realistic. These advances have allowed us to describe the protein folding in a precise manner, but our questions of how a protein folds into its specific native structure have become more hotly debated. "Old views" are often being challenged by "new views." We have reached a very exciting stage of the protein folding studies, and combination of the experimental and theoretical studies is indispensable for further clarification of the folding problem. This book thus describes the recent advances in the following topics: kinetic folding mechanisms, characterization of folding intermediates, fast folding reactions, structural stability of proteins, theory of protein folding, computer simulations, and molecular evolution in relation to protein folding. This book will appeal to researchers and graduate students of biophysics, biochemistry and molecular biology.

Audience
Researchers and graduate students of biophysics, biochemistry, and molecular biology.

Contents
Preface.

Folding Intermediates.
Folding of β-lactoglobulin, a case of the inconsistency of local and non-local interactions (Y. Goto et al.). Dynamic stability of bovine β-lactoglobulin studied by hydrogen/deuterium exchange (V. Forge et al.). Folding intermediates of equine β-lactoglobulin (M. Ikeguchi). Structural analysis of protein folding intermediates by solution X-ray scattering (M. Arai et al.). Nonnative structure of proteins and its implications for protein folding (K. Soda, Y. Seki).

Fast Folding Reactions.
Dynamics of α-helices, β-Hairpins and loops (J. Hofrichter et al.). Kinetic and structural characterization of early events in protein folding (H. Roder et al.). CD measurements on the early folding intermediate of cytochrome c using the fast flow mixer (S. Takahashi et al.). Fast protein dynamics probed by vibrational spectroscopy (Y. Mizutani, K. Yamamoto, T. Kitagawa).

Theory of Protein Folding.
The consistency principle revisited (N. Go). Complete structure reconstruction for model proteins using mutation calorimetry (M.P. Morrissey, E.I. Shakhnovich). Site resolved landscape theory of fast folding proteins (S. Takada). Hierarchy and connectivity in the folding funnel (H.K. Nakamura, M. Sasai).

Folding Mechanisms I.
The folding mechanisms of α-lactalbumin and Ca2+-binding lysozyme (K. Kuwajima et al.). Determinants of the native-like tertiary topology in the α-lactalbumin molten globule (Z.-Y. Peng). Kinetic folding reactions and molecular dynamics simulations of α-lactalbumin (T. Yoda et al.). Folding-unfolding processes of four species of 3SS-variant of lysozyme -- the role of an individual disulfide bridge (A. Yokota et al.).

Structure and Stability.
Evaluation of some factors that contribute to conformational stability of a protein using database of stability/structure (K. Yutani, K. Takano, J. Funahashi). Computational analysis of protein thermal stability and denatured state (Y. Sugita). Hydrophobic effects: roles of water and denaturants (M. Ikeguchi, S. Nakamura, K. Shimizu). Effects of deletions or insertions to the structure, stability and function of Staphylococcal nuclease (M. Kataoka, J. Yunoki, H. Takahara).

Computer Simulations.
Statistical analysis of unfolding process of protein G B1 domain with 50 runs of molecular dynamics simulations (T. Takahashi, A. Tanaka, K. Nagayama). Protein folding simulations by generalized-ensemble algorithms (Y. Okamoto).

Molecular Evolution.
Protein folding and genome evolution (M. Gō, K. Yura). Symmetry in protein folds: implication in evolution and folding (K. Kinoshita, A. Kidera, N. Go).

Folding Mechanisms II.
Multistate kinetics of folding and unfolding of barstar (A.K. Bhuyan, J.B. Udgaonkar). Equilibrium and kinetics of folding of Staphylococcal nuclease and its proline mutants (K. Maki et al.). Cold denaturation and folding/unfolding of a protein at low temperature (A. Tamura). Folding elements in dihydrofolate reductase suggested by circular permutation analysis (M. Iwakura). Thermodynamic analysis of protein induced folding upon DNA binding (M. Oda et al.). High pressure NMR study on protein dynamics and folding (K. Akasaka).

Author Index.


Bibliographic & ordering Information
Hardbound, 328 pages, publication date: NOV-1999
ISBN-13: 978-0-444-50291-9
ISBN-10: 0-444-50291-2
Imprint: EXCERPTA MEDICA
Price: Order form
GBP 86
USD 129
EUR 129

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Last update: 8 Jul 2008
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